S642A:FLUOROCITRATE complex of aconitase. Determined by X-ray diffraction at 2.5 Å resolution. Released 18 Nov 1999.
Explore 1B0K in 3D Show helices and sheets RCSB PDB PDBe
1B0K contains 40 α-helices and 52 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 1 |
| β-strand | 15 | 1 | 1 |
| α-helix | 18-32 | 15 | |
| α-helix | 38-45 | 8 | |
| β-strand | 47 | 1 | 2 |
| β-strand | 61-64 | 4 | 2 |
| β-strand | 68-72 | 5 | 3 |
| α-helix | 73-86 | 14 | |
| β-strand | 95-98 | 4 | 3 |
| β-strand | 105 | 1 | 4 |
| α-helix | 109-119 | 11 | |
| α-helix | 121-134 | 14 | |
| β-strand | 137-139 | 3 | 3 |
| α-helix | 140 | 1 | |
| β-strand | 144 | 1 | 5 |
| α-helix | 146-153 | 8 | |
| β-strand | 160-164 | 5 | 3 |
| α-helix | 168-174 | 7 | |
| β-strand | 177-180 | 4 | 3 |
| α-helix | 183-190 | 8 | |
| α-helix | 193-194 | 2 | |
| β-strand | 195-198 | 4 | 2 |
| α-helix | 199-200 | 2 | |
| β-strand | 201-208 | 8 | 6 |
| α-helix | 217-228 | 12 | |
| β-strand | 234 | 1 | 7 |
| β-strand | 236-241 | 6 | 6 |
| α-helix | 243-247 | 5 | |
| α-helix | 250-258 | 9 | |
| α-helix | 259-263 | 5 | |
| β-strand | 265 | 1 | 7 |
| β-strand | 267-269 | 3 | 6 |
| α-helix | 274-282 | 9 | |
| α-helix | 286-293 | 8 | |
| α-helix | 296-298 | 3 | |
| α-helix | 301-302 | 2 | |
| α-helix | 305-307 | 3 | |
| β-strand | 309-314 | 6 | 6 |
| β-strand | 321-323 | 3 | 8 |
| β-strand | 331-333 | 3 | 8 |
| α-helix | 337-344 | 8 | |
| β-strand | 349 | 1 | 9 |
| β-strand | 350-355 | 6 | 8 |
| α-helix | 363-378 | 16 | |
| β-strand | 386-389 | 4 | 8 |
| β-strand | 393 | 1 | 5 |
| α-helix | 394-402 | 9 | |
| α-helix | 405-411 | 7 | |
| β-strand | 414-416 | 3 | 8 |
| α-helix | 422-425 | 4 | |
| β-strand | 428 | 1 | 4 |
| β-strand | 439-443 | 5 | 8 |
| β-strand | 459-463 | 5 | 8 |
| α-helix | 466-475 | 10 | |
| β-strand | 477 | 1 | 9 |
| β-strand | 487-488 | 2 | 10 |
| β-strand | 494-495 | 2 | 10 |
| α-helix | 497-500 | 4 | |
| α-helix | 509-511 | 3 | |
| β-strand | 517-518 | 2 | 3 |
| α-helix | 519-521 | 3 | |
| β-strand | 538 | 1 | 11 |
| α-helix | 543-547 | 5 | |
| β-strand | 552-560 | 9 | 12 |
| β-strand | 561 | 1 | 13 |
| β-strand | 566 | 1 | 14 |
| α-helix | 567-570 | 4 | |
| α-helix | 574-579 | 6 | |
| β-strand | 581 | 1 | 11 |
| α-helix | 583-586 | 4 | |
| α-helix | 587-589 | 3 | |
| β-strand | 595-596 | 2 | 13 |
| β-strand | 601-602 | 2 | 13 |
| β-strand | 605-606 | 2 | 15 |
| β-strand | 613-614 | 2 | 15 |
| α-helix | 616-625 | 10 | |
| β-strand | 630-633 | 4 | 12 |
| β-strand | 638 | 1 | 16 |
| β-strand | 640 | 1 | 14 |
| α-helix | 646-653 | 8 | |
| β-strand | 656-661 | 6 | 12 |
| β-strand | 664 | 1 | 16 |
| α-helix | 666-674 | 9 | |
| β-strand | 678-682 | 5 | 12 |
| α-helix | 685-690 | 6 | |
| β-strand | 696-700 | 5 | 12 |
| β-strand | 706 | 1 | 17 |
| β-strand | 709 | 1 | 17 |
| β-strand | 711-716 | 6 | 12 |
| β-strand | 724-728 | 5 | 12 |
| α-helix | 733-741 | 9 | |
| α-helix | 744-751 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (aconitase) | A | protein | 753 | Sus scrofa | P16276 (AlphaFold model) |
>1B0K_1 PROTEIN (ACONITASE) (chains A) RAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKTY LRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQ EVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGV GGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYH GPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVP DPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNS SYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANAC GPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFN PETDFLTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDSSGQRVDVSPTSQRLQLL EPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRK ANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRAIIT KSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPGKPLKCIIKHPNGT QETILLNHTFNETQIEWFRAGSALNRMKELQQK
The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex. Lloyd, S.J., Lauble, H., Prasad, G.S. et al. Protein Sci (1999) 8:2655-2662. PubMed
Other PDB entries of the same protein (UniProt P16276 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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